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Titolo:
ACTIVATION OF THE TOBACCO SIP KINASE BY BOTH A CELL WALL-DERIVED CARBOHYDRATE ELICITOR AND PURIFIED PROTEINACEOUS ELICITINS FROM PHYTOPHTHORA SPP
Autore:
ZHANG SQ; DU H; KLESSIG DF;
Indirizzi:
RUTGERS STATE UNIV,WAKSMAN INST,190 FRELINGHUYSEN RD PISCATAWAY NJ 08854 RUTGERS STATE UNIV,WAKSMAN INST PISCATAWAY NJ 08854 RUTGERS STATE UNIV,DEPT MOL BIOL & BIOCHEM PISCATAWAY NJ 08854
Titolo Testata:
The Plant cell
fascicolo: 3, volume: 10, anno: 1998,
pagine: 435 - 449
SICI:
1040-4651(1998)10:3<435:AOTTSK>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
SIGNAL-REGULATED KINASE; MAP KINASE; FUNGAL ELICITOR; PLANT-CELLS; ARABIDOPSIS-THALIANA; ACQUIRED-RESISTANCE; SALICYLIC-ACID; PARSLEY CELLS; DEFENSE GENES; GROWTH-FACTOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
61
Recensione:
Indirizzi per estratti:
Citazione:
S.Q. Zhang et al., "ACTIVATION OF THE TOBACCO SIP KINASE BY BOTH A CELL WALL-DERIVED CARBOHYDRATE ELICITOR AND PURIFIED PROTEINACEOUS ELICITINS FROM PHYTOPHTHORA SPP", The Plant cell, 10(3), 1998, pp. 435-449

Abstract

Two purified proteinaceous fungal elicitors, parasiticein (an alpha elicitin) and cryptogein (a beta elicitin), as well as a fungal cell wall-derived carbohydrate elicitor all rapidly activated a 48-kD kinase in tobacco suspension cells. The maximum activation of this kinase paralleled or preceded medium alkalization and activation of the defense gene phenylalanine ammonia-lyase (PAL). In addition, the two elicitins, which also induced hypersensitive cell death, activated a 44- and a 40-kD kinase with delayed kinetics. By contrast, the cell wall-derivedelicitor only weakly activated the 44-kD kinase and failed to activate the 40-kD kinase. The size and substrate preference of the 48-kD kinase are reminiscent of the recently purified and cloned salicylic acid-induced protein (SIP) kinase, which is a member of the mitogen-activated protein kinase family. Antibodies raised against a peptide corresponding to the unique N terminus of SIP kinase immunoreacted with the 48-kD kinase activated by all three elicitors from Phytophthora spp. Inaddition, the cell wall elicitor and the salicylic acid-activated 48-kD kinase copurified through several chromatography steps and comigrated on two-dimensional gels. Based on these results, all three fungal elicitors appear to activate the SIP kinase. In addition, inhibition ofSIP kinase activation by kinase inhibitors correlated with the suppression of cell wall elicitor-induced medium alkalization and PAL gene activation, suggesting a regulatory function for the SIP kinase in these defense responses.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/03/20 alle ore 19:32:17